ID A0A0N1AMW1_9SPHN Unreviewed; 839 AA.
AC A0A0N1AMW1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:KPF56492.1};
GN ORFNames=IP65_01395 {ECO:0000313|EMBL:KPF56492.1};
OS Novosphingobium sp. AAP1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523413 {ECO:0000313|EMBL:KPF56492.1, ECO:0000313|Proteomes:UP000037880};
RN [1] {ECO:0000313|EMBL:KPF56492.1, ECO:0000313|Proteomes:UP000037880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP1 {ECO:0000313|EMBL:KPF56492.1,
RC ECO:0000313|Proteomes:UP000037880};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPF56492.1}.
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DR EMBL; LJHO01000001; KPF56492.1; -; Genomic_DNA.
DR RefSeq; WP_054130509.1; NZ_LJHO01000001.1.
DR AlphaFoldDB; A0A0N1AMW1; -.
DR STRING; 1523413.IP65_01395; -.
DR PATRIC; fig|1523413.3.peg.286; -.
DR OrthoDB; 9758603at2; -.
DR Proteomes; UP000037880; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR048230; GalA-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; NF041462; GalA; 1.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF18565; Glyco_hydro2_C5; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000037880};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..839
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005866051"
FT DOMAIN 101..243
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 263..359
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 369..609
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 662..717
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 732..833
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 839 AA; 90056 MW; 6DC73F21492EF2DC CRC64;
MTISPSTDRR TALALGLAGL ATSAAPALAA TAKTALTTPA ADAAASPRRR VRLADGWRFA
LGHAADMDRD FDFGRYQRTY AKPGFDVSPA TLPDFDDSAW ASVRVPHDWA VELPYAPPKA
PVPKDKEDMA AAHGFRAIGR DFPQNSVGWY RCKLPVGAGG GLVERGRAIW LEFDGVFRDC
KVFVNGYEAG GSASGYAPFR VDIADFLDYD GGPNQLTLRV DASLGEGWFY EGAGIYRHVD
LVSAAPIHVP QWGTCVRSAV DCTGAQIAIA TTLANAAEVA GTAQLRHRVL APDGREVAAI
AAQPAATLAP GAQTTLDQAL ALPAPQLWSP ETPRLYTLET SVLVDGQEID RTQTRFGIRT
LSFDGTRGFA VNGKPVKLLG VCNHQDHAGV GTAIPDALHA WRVAQTQSMG ANAWRSAHNP
PAQALLDICD ATGMMMVAET RLNTTNPEAM DELDRMILSS RNHPAIILWS VGNEEGHQGT
ERGRRISAQL VARCKQLDPT RLTTQAMDKG WDGGAADAVD VVGFNYRTDK IPAWRQRHPG
KPVIGTETAS TVATRGAYAN DAAAHVVRAY DTEHPWWAST AEEWWQIVAA EPGIAGGFIW
TGFDYRGEPT PYAQFPSVSS YFGAMDLCGF PKDNYYYYRA WWRRDAPLVH LLPHWNWAGR
EGQPIEVWVH GNCAEVELLL NGRSLGRKAM PQNGHLAWMV PYAPGRIEAR GYNHGRLAAR
DSRVTAGKPA ALRLSADRTR LAADGGDTAA VRVEVIDAAG NLVPMADTAI DFSLSGAARI
IGLGNGNPTS TEPDKGHARR AFNGLAQALV QSAGTAGAAR LTVTAAGLAP ASLDLFFHA
//
